Discovery and functional analysis of a 4th electron-transferring tryptophan conserved exclusively in animal cryptochromes and (6-4) photolyases. Issue 85 (10th September 2015)

• Record Type: Journal Article
• Authors: Müller, Pavel; Yamamoto, Junpei; Martin, Ryan; Iwai, Shigenori; Brettel, Klaus
• Is Part Of: Chemical communications. Volume 51:Issue 85(2015)
• Page Start: 15502
• Page End: 15505
• Publication Date: 2015-09-10
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c5cc06276d
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : A previously ignored 4th tryptophan is involved in light-induced electron transfer in animal cryptochromes and (6-4) photolyases. Its presence leads to a much longer-lived FAD˙ − TrpH˙ + radical pair than in other related proteins. Consequences for animal magnetoreception are discussed. Abstract : A 4th electron transferring tryptophan in animal cryptochromes and (6-4) photolyases is discovered and functionally analyzed by transient absorption. It yields a much longer-lived flavin-tryptophan radical pair than the mere tryptophan triad in related flavoproteins, questioning the putative role of the primary light reaction of cryptochrome in animal magnetoreception.